Multiscale Mechanics of Fibrin Polymer: Gel Stretching with Protein Unfolding and Loss of Water

Author:

Brown André E. X.12,Litvinov Rustem I.3,Discher Dennis E.24,Purohit Prashant K.5,Weisel John W.3

Affiliation:

1. Department of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA 19104, USA.

2. Nano/Bio Interface Center, University of Pennsylvania, Philadelphia, PA 19104, USA.

3. Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.

4. Graduate Groups in Physics and Cell Biology and Physiology, University of Pennsylvania, Philadelphia, PA 19104, USA.

5. Department of Mechanical Engineering and Applied Mechanics, University of Pennsylvania, Philadelphia, PA 19104, USA.

Abstract

<< Focusing on Fibrin Vascular injury initiates biochemical reactions that cause the blood protein, fibrin, to polymerize and help to stop bleeding and support wound healing. Fibrin can also be a scaffold for thrombi that lead to cardiovascular diseases. To maintain homeostasis, fibrin clots must be stiff, plastic, and, so that the network can be decompsed, permeable. Brown et al. (p. 741 ) investigated the behavior of fibrin clots at the macroscopic, single-fiber, and molecular scale. At relatively low strains, fibers aligned and formed bundles, and at higher strains, protein unfolding occurred. An integrated model provides a molecular basis for fibrin elasticity and extensibility.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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